ID   RECD_BUCAP              Reviewed;         602 AA.
AC   Q8K9A8;
DT   08-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   03-AUG-2022, entry version 111.
DE   RecName: Full=RecBCD enzyme subunit RecD {ECO:0000255|HAMAP-Rule:MF_01487};
DE            EC=3.1.11.5 {ECO:0000255|HAMAP-Rule:MF_01487};
DE   AltName: Full=Exonuclease V subunit RecD {ECO:0000255|HAMAP-Rule:MF_01487};
DE            Short=ExoV subunit RecD {ECO:0000255|HAMAP-Rule:MF_01487};
DE   AltName: Full=Helicase/nuclease RecBCD subunit RecD {ECO:0000255|HAMAP-Rule:MF_01487};
GN   Name=recD {ECO:0000255|HAMAP-Rule:MF_01487}; OrderedLocusNames=BUsg_440;
OS   Buchnera aphidicola subsp. Schizaphis graminum (strain Sg).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Buchnera.
OX   NCBI_TaxID=198804;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Sg;
RX   PubMed=12089438; DOI=10.1126/science.1071278;
RA   Tamas I., Klasson L., Canbaeck B., Naeslund A.K., Eriksson A.-S.,
RA   Wernegreen J.J., Sandstroem J.P., Moran N.A., Andersson S.G.E.;
RT   "50 million years of genomic stasis in endosymbiotic bacteria.";
RL   Science 296:2376-2379(2002).
CC   -!- FUNCTION: A helicase/nuclease that prepares dsDNA breaks (DSB) for
CC       recombinational DNA repair. Binds to DSBs and unwinds DNA via a highly
CC       rapid and processive ATP-dependent bidirectional helicase activity.
CC       Unwinds dsDNA until it encounters a Chi (crossover hotspot instigator)
CC       sequence from the 3' direction. Cuts ssDNA a few nucleotides 3' to the
CC       Chi site. The properties and activities of the enzyme are changed at
CC       Chi. The Chi-altered holoenzyme produces a long 3'-ssDNA overhang and
CC       facilitates RecA-binding to the ssDNA for homologous DNA recombination
CC       and repair. Holoenzyme degrades any linearized DNA that is unable to
CC       undergo homologous recombination. In the holoenzyme this subunit has
CC       ssDNA-dependent ATPase and 5'-3' helicase activity. When added to pre-
CC       assembled RecBC greatly stimulates nuclease activity and augments
CC       holoenzyme processivity. Negatively regulates the RecA-loading ability
CC       of RecBCD. {ECO:0000255|HAMAP-Rule:MF_01487}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Exonucleolytic cleavage (in the presence of ATP) in either
CC         5'- to 3'- or 3'- to 5'-direction to yield 5'-
CC         phosphooligonucleotides.; EC=3.1.11.5; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_01487};
CC   -!- SUBUNIT: Heterotrimer of RecB, RecC and RecD. All subunits contribute
CC       to DNA-binding. {ECO:0000255|HAMAP-Rule:MF_01487}.
CC   -!- SIMILARITY: Belongs to the RecD family. {ECO:0000255|HAMAP-
CC       Rule:MF_01487}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AE013218; AAM67983.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q8K9A8; -.
DR   SMR; Q8K9A8; -.
DR   STRING; 198804.BUsg_440; -.
DR   EnsemblBacteria; AAM67983; AAM67983; BUsg_440.
DR   KEGG; bas:BUsg_440; -.
DR   eggNOG; COG0507; Bacteria.
DR   HOGENOM; CLU_007524_1_2_6; -.
DR   OMA; MIDLEMM; -.
DR   Proteomes; UP000000416; Chromosome.
DR   GO; GO:0009338; C:exodeoxyribonuclease V complex; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003678; F:DNA helicase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0008854; F:exodeoxyribonuclease V activity; IEA:UniProtKB-EC.
DR   GO; GO:0000724; P:double-strand break repair via homologous recombination; IEA:UniProtKB-UniRule.
DR   Gene3D; 1.10.10.1020; -; 1.
DR   Gene3D; 3.40.50.300; -; 3.
DR   HAMAP; MF_01487; RecD; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR006344; RecD.
DR   InterPro; IPR041851; RecD_N.
DR   InterPro; IPR027785; UvrD-like_helicase_C.
DR   Pfam; PF13538; UvrD_C_2; 1.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR01447; recD; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
PE   3: Inferred from homology;
KW   ATP-binding; DNA damage; DNA repair; DNA-binding; Exonuclease; Helicase;
KW   Hydrolase; Nuclease; Nucleotide-binding.
FT   CHAIN           1..602
FT                   /note="RecBCD enzyme subunit RecD"
FT                   /id="PRO_0000087113"
FT   BINDING         174..181
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01487"
SQ   SEQUENCE   602 AA;  70408 MW;  072600F2A570A253 CRC64;
     MNMSHLLQNF ANKKIITLVD FYFSQFISKK NSIIMLISAC VSFESKNGHI FLPIEYFEKN
     CFFSISNKQF INKILKCLNK KKINWSLELS EHISCGDGSI ITPLVFYKDK IYLYKIWKAE
     KKILERLYEK NQFDTIDTQQ CLNILNNLFS KKKHDLQKIA VILTLINNII FITGGPGTGK
     TTIILKIIIA LIKNAKKKIK IQLSAPTGKA TENLIEILND KWLNRYLLKE EKKQFSFNPI
     MTIHQLLGIS KKSEKIFFNK NNLLMIDILI IDEASMIDIL MMSNILSALS KKTKIIFIGD
     HNQLKPVKSS SILKYICSYA EDGYSLKTQS ILQEITQNSI INYKINKKNT SYISDKICVL
     KKSYRFEKKT GIYILSNAVY NKETKIFEKL FKNSIENVFF YEINSEIEYK KMINIIINNN
     KIFWRKIYEK KNIKEIIKTF KNHQILCIVK NGFFGVNFIN KILEEEMYKR NIFNKRFYIN
     NKLWYIGKPI IITENNQCLG IFNGEIGITN LSQKNTLQVS FLKKDNFIEN IPIEILKNYK
     TSWSITVHKA QGSEFNNISL ILPNKNLKIL KKDILYTGIT RTRKQLNIFS TKEIFIKTVL
     KN